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Protein folding intermediates versus unfolded state ensembles

Reference	B11984
Principal Investigator / Supervisor	Professor Jon Waltho
Co-Investigators / Co-Supervisors	Professor Anthony Clarke
Institution	University of Sheffield
Department	Molecular Biology and Biotechnology
Funding type	Research
Value (£)	239,924
Status	Completed
Type	Research Grant
Start date	17/11/1999
End date	01/02/2003
Duration	39 months

Abstract

In the proposed study we will determine the relationship between polymer-like random collapse and the formation of topologically native-like Ikin states that accelerates the folding of PGK. We will quantify the extent of structure in the Ikin states of both domains of intact PGK; determine the stability of hydrogen bonds in the Ikin state of the isolated N-domain; identify and characterise transitions within the U state of the N-domain on dilution of denaturant; distinguish the roles of random collapsed U' states and topologically organised Ikin states. The incorporation of NMR-derived backbone information for the intact protein with a novel protein engineering based assessment of the role of sidechains in the formation of kinetic intermediate states, would provide the first high resolution picture of the folding of a large, two domain protein.

Summary

unavailable

Committee	Closed Committee - Biomolecular Sciences (BMS)
Research Topics	X – not assigned to a current Research Topic
Research Priority	X – Research Priority information not available
Research Initiative	X - not in an Initiative
Funding Scheme	X – not Funded via a specific Funding Scheme

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